2x2e

DYNAMIN GTPASE DIMER, LONG AXIS FORM
Publication Abstract from Nature Dynamin is an atypical GTPase that catalyses membrane fission during clathrin-mediated endocytosis. The mechanisms of dynamin’s basal and assembly-stimulated GTP hydrolysis are unknown, though both are indirectly influenced by the GTPase effector domain (GED). Here we present the 2.0 Å resolution crystal structure of a human dynamin 1-derived minimal GTPase–GED fusion protein, which was dimeric in the presence of the transition state mimic GDP.AlF4-.The structure reveals dynamin’s catalytic machinery and explains how assembly-stimulated GTP hydrolysis is achieved through G domain dimerization. A sodium ion present in the active site suggests that dynamin uses a cation to compensate for the developing negative charge in the transition state in the absence of an arginine finger. Structural comparison to the rat dynamin G domain reveals key conformational changes that promote G domain dimerization and stimulated hydrolysis. The structure of the GTPase–GED fusion protein dimer provides insight into the mechanisms underlying dynamin-catalysed membrane fission.

''G domain dimerization controls dynamin's assembly-stimulated GTPase activity., Chappie JS, Sharmistha A, Leonard M, Schmid SL, Dyda Fred, Nature. 2010 Published online 28 April 2010. Article''

About this Structure
2X2E is a 2 chains structure with sequences from Homo sapiens. Full crystallographic information is available from OCA.

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